## Abstract Porous silicon (pβSi) has been investigated as a novel delivery system for protein therapeutics. The loading of a model hydrophilic protein, Papain into anodised and stain etched pβSi powders has been investigated using Xβray photoelectron spectroscopy (XPS) and infrared spectroscopy (F
Peptide and protein loading into porous silicon wafers
β Scribed by Prestidge, C. A. ;Barnes, T. J. ;Mierczynska-Vasilev, A. ;Kempson, I. ;Peddie, F. ;Barnett, C.
- Book ID
- 105364440
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 232 KB
- Volume
- 205
- Category
- Article
- ISSN
- 0031-8965
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β¦ Synopsis
Abstract
The influence of peptide/protein size and hydrophobicity on the physical and chemical aspects of loading within porous silicon (pSi) wafer samples has been determined using Atomic Force Microscopy (AFM) and TimeβofβFlight Secondary Ion Mass Spectroscopy (ToFβSIMS). Both Gramicidin A (a small hydrophobic peptide) and Papain (a larger hydrophilic protein) were observed (ToFβSIMS) to penetrate across the entire pSi layer, even at low loading levels. AFM surface imaging of pSi wafers during peptide/protein loading showed that surface roughness increased with Papain loading, but decreased with Gramicidin A loading. For Papain, the loading methodology was also found to influence loading efficiency. These differences indicate more pronounced surface adsorption of Papain. (Β© 2008 WILEYβVCH Verlag GmbH & Co. KGaA, Weinheim)
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